Complete 1H and 13C assignment of Lys and Leu sidechains of staphylococcal nuclease using HCCH‐COSY and HCCH‐TOCSY 3D NMR spectroscopy

FEBS Letters

Torchia, D.A.¹  Sparks, S.W.¹  Baldisseri, D.M.¹  Pelton, J.G.¹ 

[1]Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Staphylococcal nuclease;    Sidechain structure;    Assignment;    3D NMR;    COSY;    correlated spectroscopy;    TOCSY;    total related spectroscopy;    HCCH-COSY;    3D 1H- 13C- 13C- 1H correlation spectroscopy via Jcc carbon couplings;    HCCH-TOCSY;    3D 1H- 13C- 13C- 1H total correlation spectroscopy with isotropic mixing of 13C magnetization;    NMR;    nuclear magnetic resonance;    NOESY;    2D nuclear Overhauser effect spectroscopy;    HMQC;    heteronuclear;    multiple quantum correlation spectroscopy;    HOHAHA;    homonuclear Hartmann-Hahn spectroscopy;    DANTE;    delays alternating with nutation for tailored excitation;    DIPSI;    decouping in the presence of scalar interactions;   

DOI  :  10.1016/0014-5793(91)80352-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complete proton and carbon sidechain assignments are reported for 22 lysine and II leucine residues in staphylococcal nuclease, an enzyme with 149 residues. These assignments are readily obtained in a direct manner from the correlations observed in the 3D HCCH-COSY and HCCH-TOCSY spectra and the unknown protein backbone assignments. These assignments open the way to detailed of the sidechain structure and dynamics at the active site, in the hydrophobic core and on the surface of the protein.

【 授权许可】

Unknown